Information on EC 1.14.18.3 - methane monooxygenase (particulate)

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY
1.14.18.3
-
RECOMMENDED NAME
GeneOntology No.
methane monooxygenase (particulate)
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O
show the reaction diagram
mechanism
-
methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O
show the reaction diagram
mechanism of pMMO
-
methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O
show the reaction diagram
mechanism of pMMO
Methylococcus capsulatus Bath
-
-
methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
-
methane + quinol + O2 = methanol + quinone + H2O
show the reaction diagram
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Metabolic pathways
-
Methane metabolism
-
methane oxidation to methanol II
-
SYSTEMATIC NAME
IUBMB Comments
methane,quinol:oxygen oxidoreductase
Contains copper. It is membrane-bound, in contrast to the soluble methane monooxygenase (EC 1.14.13.25).
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
membrane-associated methane monooxygenase
-
-
membrane-associated methane monooxygenase
Methylococcus capsulatus Bath
-
-
-
membrane-bound methane monooxygenase
-
-
membrane-bound methane monooxygenase
Methylococcus capsulatus M
-
-
-
methane hydroxylase
-
-
methane hydroxylase
Methylococcus capsulatus M
-
-
-
MMO
Methylococcus capsulatus Bath, Methylococcus capsulatus M
-
-
-
MMO
Methylosinus trichosporium IMV 3011
-
-
-
particulate methane mono-oxygenase
Q49104
-
particulate methane mono-oxygenase
-
-
particulate methane monooxygenase
-
-
particulate methane monooxygenase
Methylococcus capsulatus ATCC 33009, Methylococcus capsulatus Bath
-
-
-
particulate methane monooxygenase
-
-
particulate methane monooxygenase
Methylocystis sp.
-
-
particulate methane monooxygenase
-
-
-
particulate methane monooxygenase
-
-
particulate methane monooxygenase
-
-
-
particulate methane monooxygenase
Q25BV2 and Q25BV3 and Q25BV4
-
particulate methane monooxygenase
Methylomicrobium japanense NI
Q25BV2 and Q25BV3 and Q25BV4
-
-
particulate methane monooxygenase
-
-
particulate methane monooxygenase
-
-
particulate methane monooxygenase
-
-
particulate methane monooxygenase
E1CBW9, E1CBX0, E1CBX1
-
particulate methane monooxygenase
E1CBW9, E1CBX0, E1CBX1
-
-
particulate methane monooxygenase
Soil bacterium
-
-
particulate methane monooxygenase
Q1EPW5, Q1EPW6
-
particulate methane monooxygenase A
D0FK34, D0FK37, D0FK39, D0FK43, D0FK44, D0FK45, D0FK53, D0FK57, D0FK58, D0FK59, D0FK61, D0FK62, D0FK63, D0FK65, D0FK67, D0FKJ4, D0FKK3, D0FKS0, D0FL26, D0FL48
-
particulate methane-oxidizing complex
-
-
particulate methane-oxidizing complex
Methylococcus capsulatus Bath
-
-
-
PMH
Methylococcus capsulatus M
-
-
-
pMMO
-
consists of two protein components: NADH oxidoreductase (pMMOR) and hydroxylase (pMMOH)
pMMO
-
particulate, membrane-bound enzyme form
pMMO
Methylococcus capsulatus ATCC 33009
-
-
-
pMMO
Methylococcus capsulatus Bath
-
particulate, membrane-bound enzyme form
-
pMMO
Methylococcus capsulatus M
-
; consists of two protein components: NADH oxidoreductase (pMMOR) and hydroxylase (pMMOH)
-
pMMO
Methylocystis sp.
-
-
pMMO
-
-
-
pMMO
Q25BV2 and Q25BV3 and Q25BV4
-
pMMO
Methylomicrobium japanense NI
Q25BV2 and Q25BV3 and Q25BV4
-
-
pMMO
-
particulate, membrane-bound enzyme form
pMMO
Methylosinus trichosporium IMV 3011
-
particulate, membrane-bound enzyme form
-
pMMO
E1CBW9, E1CBX0, E1CBX1
-
pMMO
E1CBW9, E1CBX0, E1CBX1
-
-
pMMO
Soil bacterium
-
-
pMMO hydroxylase
-
-
pMMO hydroxylase
Methylococcus capsulatus Bath
-
-
-
pMMO-H
Methylococcus capsulatus Bath
-
-
-
pMMO1
Methylocystis sp.
-
isozyme, pMMO1 oxidizes methane at higher mixing ratios than pMMO2
pMMO1
-
isozyme, pMMO1 oxidizes methane at higher mixing ratios than pMMO2
-
pMMO2
Methylocystis sp.
-
isozyme, pMMO2 oxidizes methane at lower mixing ratios than pMMO1
pMMO2
-
isozyme, pMMO2 oxidizes methane at lower mixing ratios than pMMO1
-
PmoA
Soil bacterium
-
-
PmoA
D0FK34, D0FK37, D0FK39, D0FK43, D0FK44, D0FK45, D0FK53, D0FK57, D0FK58, D0FK59, D0FK61, D0FK62, D0FK63, D0FK65, D0FK67, D0FKJ4, D0FKK3, D0FKS0, D0FL26, D0FL48
-
PmoB
-
large subunit of pMMO
sMMO
-
consists of three components: hydroxylase (sMMOH), NADH-dependent reductase (sMMOR), and the regulatory protein B (sMMOB)
sMMO
-
soluble, cytoplasmic enzyme form
sMMO
Methylococcus capsulatus Bath
-
soluble, cytoplasmic enzyme form
-
sMMO
Methylococcus capsulatus M
-
consists of three components: hydroxylase (sMMOH), NADH-dependent reductase (sMMOR), and the regulatory protein B (sMMOB)
-
sMMO
Q25BV9 and Q25BW0 and Q25BW2 and Q25BW3
-
sMMO
Methylomicrobium japanense NI
Q25BV9 and Q25BW0 and Q25BW2 and Q25BW3
-
-
soluble methane monooxygenase
Q25BV9 and Q25BW0 and Q25BW2 and Q25BW3
-
soluble methane monooxygenase
Methylomicrobium japanense NI
Q25BV9 and Q25BW0 and Q25BW2 and Q25BW3
-
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Bath; enzyme form pMMO is copper-inducible
-
-
Manually annotated by BRENDA team
Methylococcus capsulatus ATCC 33009
-
-
-
Manually annotated by BRENDA team
Methylococcus capsulatus Bath
-
-
-
Manually annotated by BRENDA team
Methylococcus capsulatus Bath
Bath
-
-
Manually annotated by BRENDA team
Methylococcus capsulatus Bath
strain Bath
-
-
Manually annotated by BRENDA team
Methylococcus capsulatus HD6T
-
-
-
Manually annotated by BRENDA team
Methylococcus capsulatus M
strain M
-
-
Manually annotated by BRENDA team
Methylocystis sp.
-
-
-
Manually annotated by BRENDA team
Methylocystis sp.
strain Sc2
-
-
Manually annotated by BRENDA team
strain Sc2
-
-
Manually annotated by BRENDA team
pMMO protein B, pMMO protein A, and pMMO protein C; strain NI
Q25BV2 and Q25BV3 and Q25BV4
UniProt
Manually annotated by BRENDA team
sMMO subunit component D and sMMO subunit gamma and sMMO subunit beta and sMMO subunit alpha; strain NI
Q25BV9 and Q25BW0 and Q25BW2 and Q25BW3
UniProt
Manually annotated by BRENDA team
Methylomicrobium japanense NI
pMMO protein B, pMMO protein A, and pMMO protein C; strain NI
Q25BV2 and Q25BV3 and Q25BV4
UniProt
Manually annotated by BRENDA team
Methylomicrobium japanense NI
sMMO subunit component D and sMMO subunit gamma and sMMO subunit beta and sMMO subunit alpha; strain NI
Q25BV9 and Q25BW0 and Q25BW2 and Q25BW3
UniProt
Manually annotated by BRENDA team
strain IMV 3011
-
-
Manually annotated by BRENDA team
Methylosinus trichosporium IMV 3011
strain IMV 3011
-
-
Manually annotated by BRENDA team
Soil bacterium
-
-
-
Manually annotated by BRENDA team
fragment; most closely related to Methylobacter sp. strain BB5.1 and Methylocaldum szegediense
UniProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,1,1-trifluoropropane + NAD(P)H + H+ + O2
(2R)-1,1,1-trifluoropropan-2-ol + (2S)-1,1,1-trifluoropropan-2-ol + NAD(P)+ + H2O
show the reaction diagram
-
-
the S stereoisomer is the dominant product
-
?
1,3-butadiene + duroquinol + O2
1,2-epoxybut-3-ene + duroquinone + H2O
show the reaction diagram
-
-
100% 1,2-epoxybut-3-ene is produced, 36% (R)-selectivity, 64% (S)-selectivity
-
?
1-bromopropane + duroquinol + O2
1-bromo-2-propanol + 1-propanol + 1-bromo-3-propanol + duroquinone + H2O
show the reaction diagram
-
-
72% 1-bromo-2-propanol (70% (R)-selectivity, 30% (S)-selectivity), 24% 1-propanol and 4% 1-bromo-3-propanol are produced
-
?
1-bromopropene + duroquinol + O2
1-bromo-2,3-epoxypropane + allyl-alcohol + 1-propanol + duroquinone + H2O
show the reaction diagram
-
-
63% 1-bromo-2,3-epoxypropane, 31% allyl-alcohol and 6% 1-propanol are produced
-
?
1-butene + duroquinol + O2
1,2-epoxybutane + duroquinone + H2O
show the reaction diagram
-
-
100% epoxybutane is produced, 36% (R)-selectivity, 64% (S)-selectivity
-
?
1-butene + NAD(P)H + H+ + O2
1,2-epoxybutane + NAD(P)+ + H2O
show the reaction diagram
-
-
-
-
?
1-butene + NAD(P)H + H+ + O2
3-buten-2-ol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
-
?
1-chloropropane + duroquinol + O2
1-chloro-2-propanol + 1-propanol + 1-chloro-3-propanol + duroquinone + H2O
show the reaction diagram
-
-
64% 1-chloro-2-propanol (70% (R)-selectivity, 30% (S)-selectivity), 29% 1-propanol and 7% 1-chloro-3-propanol are produced
-
?
1-chloropropene + duroquinol + O2
1-chloro-2,3-epoxypropane + allyl-alcohol + 1-propanol + duroquinone + H2O
show the reaction diagram
-
-
67% 1-chloro-2,3-epoxypropane, 23% allyl-alcohol and 10% 1-propanol are produced
-
?
2-bromopropane + duroquinol + O2
2-bromo-1-propanol + acetone + duroquinone + H2O
show the reaction diagram
-
-
2-bromo-1-propanol shows 26% (R)-selectivity and 74% (S)-selectivity
-
?
2-chloropropane + duroquinol + O2
2-chloro-1-propanol + ? + duroquinone + H2O
show the reaction diagram
-
-
1-chloro-2-propanol shows 26% (R)-selectivity and 74% (S)-selectivity
-
?
3,3,3-trifluoroprop-1-ene + NAD(P)H + H+ + O2
(2S)-2-(trifluoromethyl)oxirane + (2R)-2-(trifluoromethyl)oxirane + NAD(P)+ + H2O
show the reaction diagram
-
-
the S stereoisomer is the dominant product
-
?
3,3,3-trifluoropropene + NAD(P)H + H+ + O2
?
show the reaction diagram
-
-
-
-
?
butane + duroquinol + O2
2-butanol + butanal + duroquinone + H2O
show the reaction diagram
-
-
91% 2-butanal and 9% butanal are produced
-
?
butane + NAD(P)H + H+ + O2
1-butanol + 2-butanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
-
?
cis-2-butene + duroquinol + O2
cis-2,3-epoxybutane + duroquinone + H2O
show the reaction diagram
-
-
cis-2,3-epoxybutane is produced
-
?
cis-2-butene + NAD(P)H + H+ + O2
cis-2,3-epoxybutane + cis-2-buten-1-ol + 2-butanone + NAD(P)+ + H2O
show the reaction diagram
-
-
-
-
?
cis-but-2-ene + NAD(P)H + H+ + O2
cis-2,3-dimethyloxiran + NAD(P)+ + H2O
show the reaction diagram
-
-
-
-
?
duroquinone + NAD(P)H + O2
duroquinol + NAD(P)+ + H2O
show the reaction diagram
Methylococcus capsulatus, Methylococcus capsulatus Bath
-
enzyme form pMMO
-
?
ethane + duroquinol + O2
ethanal + duroquinone + H2O
show the reaction diagram
-
-
100% ethanal is produced
-
?
ethylene + duroquinol + O2
epoxyethane + duroquinone + H2O
show the reaction diagram
-
-
100% epoxyethane produced
-
?
formate + NAD(P)H + O2
?
show the reaction diagram
Methylococcus capsulatus, Methylococcus capsulatus Bath
-
assay with whole cells
-
-
?
methane + duroquinol + O2
methanol + duroquinone + H2O
show the reaction diagram
-
-
-
-
?
methane + duroquinol + O2
methanol + duroquinone + H2O
show the reaction diagram
Methylomicrobium album, Methylocystis sp.
-
-
-
-
?
methane + duroquinol + O2
methanol + duroquinone + H2O
show the reaction diagram
-
-
100% methanol is produced
-
?
methane + duroquinol + O2
methanol + duroquinone + H2O
show the reaction diagram
Methylococcus capsulatus Bath
-
-
-
-
?
methane + duroquinol + O2
methanol + duroquinone + H2O
show the reaction diagram
-
-
-
-
?
methane + NAD(P)H + H+ + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
-
?
methane + NAD(P)H + H+ + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
Methylocystis sp.
-
-
-
-
?
methane + NAD(P)H + H+ + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
Q25BV2 and Q25BV3 and Q25BV4, Q25BV9 and Q25BW0 and Q25BW2 and Q25BW3
-
-
-
?
methane + NAD(P)H + H+ + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
-
?
methane + NAD(P)H + H+ + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
Methylomicrobium japanense NI
Q25BV2 and Q25BV3 and Q25BV4, Q25BV9 and Q25BW0 and Q25BW2 and Q25BW3
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
Q25BV2 and Q25BV3 and Q25BV4, Q25BV9 and Q25BW0 and Q25BW2 and Q25BW3
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
D0FK34, D0FK37, D0FK39, D0FK43, D0FK44, D0FK45, D0FK53, D0FK57, D0FK58, D0FK59, D0FK61, D0FK62, D0FK63, D0FK65, D0FK67, D0FKJ4, D0FKK3, D0FKS0, D0FL26, D0FL48
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
Q49104
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
Soil bacterium
-
pmoA cluster JR3 may be the most important methane oxidizer for arid soils
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
Methylococcus capsulatus Bath
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
Methylococcus capsulatus Bath
-
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
Methylomicrobium japanense NI
Q25BV2 and Q25BV3 and Q25BV4, Q25BV9 and Q25BW0 and Q25BW2 and Q25BW3
-
-
-
?
methane + NADH + H+ + O2
methanol + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
methane + NADH + H+ + O2
methanol + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
methane + NADH + H+ + O2
methanol + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
methane + NADH + H+ + O2
methanol + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
methane + NADH + H+ + O2
methanol + NAD+ + H2O
show the reaction diagram
Methylocystis sp.
-
-
-
-
?
methane + NADH + O2
methanol + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
methane + NADH + O2
methanol + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
methane + NADH + O2
methanol + NAD+ + H2O
show the reaction diagram
-
in the presence of pMMO substrate methane, the H2O2 formation is diminished, which is likely to be caused by the consumption of electrons by methane oxidation
-
-
?
methane + NADH + O2
methanol + NAD+ + H2O
show the reaction diagram
Methylococcus capsulatus Bath
-
-
-
-
?
methane + NADH + O2
methanol + NAD+ + H2O
show the reaction diagram
Methylococcus capsulatus M
-
-
-
-
?
pentane + duroquinol + O2
2-pentanol + pentanal + duroquinone + H2O
show the reaction diagram
-
-
31% 2-pentanal and 69% pentanal are produced
-
?
pentane + NAD(P)H + H+ + O2
1-pentanol + 2-pentanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
-
?
propane + duroquinol + O2
2-propanol + propanal + duroquinone + H2O
show the reaction diagram
-
-
84% 2-propanal and 16% propanal are produced
-
?
propane + NAD(P)H + H+ + O2
1-propanol + 2-propanol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
-
?
propene + NAD(P)H + H+ + O2
1,2-epoxypropane + NAD(P)+ + H2O
show the reaction diagram
-
-
-
-
?
propene + NADH + H+ + O2
epoxypropane + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
propene + NADH + H+ + O2
epoxypropene + NAD+ + H2O
show the reaction diagram
-
-
57% (R)-selectivity, 43% (S)-selectivity
-
?
propylene + 2,3-dimethylquinol + O2
propylene oxide + 2,3-dimethylquinone + H2O
show the reaction diagram
Methylococcus capsulatus, Methylococcus capsulatus Bath
-
-
-
-
?
propylene + coenzyme Q0 + O2
propylene oxide + reduced coenzyme Q0 + H2O
show the reaction diagram
Methylococcus capsulatus, Methylococcus capsulatus Bath
-
-
-
-
?
propylene + decyl-plastoquinol + O2
propylene oxide + decyl-plastoquinone + H2O
show the reaction diagram
Methylococcus capsulatus, Methylococcus capsulatus Bath
-
higher activity compared to duroquinol
-
-
?
propylene + decylubiquinol + O2
propylene oxide + decylubiquinone + H2O
show the reaction diagram
Methylococcus capsulatus, Methylococcus capsulatus Bath
-
-
-
-
?
propylene + duroquinol + O2
propylene oxide + reduced duroquinol + H2O
show the reaction diagram
Methylococcus capsulatus, Methylococcus capsulatus Bath
-
-
-
-
?
propylene + duroquinol + O2
propylene epoxide + duroquinone + H2O
show the reaction diagram
Methylococcus capsulatus, Methylococcus capsulatus Bath
-
-
-
-
?
propylene + duroquinol + O2
epoxypropane + allyl-alcohol + 1-propanol + duroquinone + H2O
show the reaction diagram
-
-
95% epoxypropane, 4.6% allyl-alcohol and 0.4% butanal are produced
-
?
propylene + duroquinol + O2
propylene oxide + duroquinone + H2O
show the reaction diagram
-
-
-
-
?
propylene + duroquinol + O2
propylene oxide + duroquinone + H2O
show the reaction diagram
Methylococcus capsulatus Bath
-
-
-
-
?
propylene + duroquinol + O2
propylene oxide + duroquinone + H2O
show the reaction diagram
Methylococcus capsulatus ATCC 33009
-
-
-
-
?
propylene + menauinol + O2
propylene oxide + menaquinone + H2O
show the reaction diagram
-
-
-
-
?
propylene + NAD(P)H + O2
propylene oxide + NADP+ + H2O
show the reaction diagram
Methylococcus capsulatus, Methylococcus capsulatus Bath
-
enzyme form sMMO
-
?
propylene + NADH + H+ + O2
propylene oxide + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
propylene + NADH + H+ + O2
propylene oxide + NAD+ + H2O
show the reaction diagram
Methylococcus capsulatus ATCC 33009
-
-
-
-
?
propylene + NADH + O2
propylene oxide + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
propylene + NADH + O2
propylene oxide + NAD+ + H2O
show the reaction diagram
Methylococcus capsulatus M
-
-
-
-
?
propylene + NADH + O2
propylene oxide + NADP+ + H2O
show the reaction diagram
Methylococcus capsulatus, Methylococcus capsulatus Bath
-
-
-
-
?
propylene + NADH + O2
propylene epoxide + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
propylene + NADH + O2
propylene epoxide + NAD+ + H2O
show the reaction diagram
Methylococcus capsulatus Bath
-
-
-
-
?
propylene + trimethylquinol + O2
propylene oxide + trimethylquinone + H2O
show the reaction diagram
-
-
-
-
?
trans-2-butene + duroquinol + O2
trans-2,3-epoxybutane + trans-2-butane-1-al + duroquinone + H2O
show the reaction diagram
-
-
41% trans-2,3-epoxybutane and 59% trans-2-butane-1-al are produced
-
?
trans-2-butene + NAD(P)H + H+ + O2
trans-2,3-epoxybutane + trans-2-buten-1-ol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
-
?
trans-but-2-ene + NAD(P)H + H+ + O2
(2R,3R)-trans-2,3-dimethyloxirane + (2S,3S)-trans-2,3-dimethyloxirane + NAD(P)+ + H2O
show the reaction diagram
-
-
the S,S stereoisomer is the dominant product
-
?
methane + trans-dichloroethylene + vinyl chloride + trichloroethylene + O2
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
duroquinol, an electron donor for pMMO may induce the formation of H2O2 by pMMO under aerobic conditions
-
-
-
additional information
?
-
-
unlike the sMMO, the pMMO enzyme has relatively narrow substrate specificity, oxidising alkanes and alkenes of up to five carbons but not aromatic compounds
-
-
-
additional information
?
-
-
decyl-plastoquinol, reduced coenzyme Q1, and trimethylquinol can drive pMMO, though its activity is lower than that with duroquinol. Succinate-driven pMMO activity in the membrane fractions is also observed
-
-
-
additional information
?
-
-
pMMO cannot oxidize naphthalene
-
-
-
additional information
?
-
-
pMMO has narrower substrate specificity but higher activity with smaller hydrocarbons like methane, ethane, and propene compared to sMMO
-
-
-
additional information
?
-
-
quinols are effective reductants for the detergent-solubilized enzyme, whereas NADH is ineffective
-
-
-
additional information
?
-
Methylococcus capsulatus Bath
-
unlike the sMMO, the pMMO enzyme has relatively narrow substrate specificity, oxidising alkanes and alkenes of up to five carbons but not aromatic compounds
-
-
-
additional information
?
-
Methylococcus capsulatus Bath
-
quinols are effective reductants for the detergent-solubilized enzyme, whereas NADH is ineffective
-
-
-
additional information
?
-
-
unlike the sMMO, the pMMO enzyme has relatively narrow substrate specificity, oxidising alkanes and alkenes of up to five carbons but not aromatic compounds
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
formate + NAD(P)H + O2
?
show the reaction diagram
Methylococcus capsulatus, Methylococcus capsulatus Bath
-
assay with whole cells
-
-
?
methane + duroquinol + O2
methanol + duroquinone + H2O
show the reaction diagram
-
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
Methylococcus capsulatus, Methylococcus capsulatus Bath
-
-
-
-
?
methane + NADH + H+ + O2
methanol + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
methane + NADH + O2
methanol + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
methane + NADH + O2
methanol + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
methane + NADH + O2
methanol + NAD+ + H2O
show the reaction diagram
Methylococcus capsulatus Bath
-
-
-
-
?
methane + NADH + O2
methanol + NAD+ + H2O
show the reaction diagram
Methylococcus capsulatus M
-
-
-
-
?
additional information
?
-
-
unlike the sMMO, the pMMO enzyme has relatively narrow substrate specificity, oxidising alkanes and alkenes of up to five carbons but not aromatic compounds
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
NADH
Q25BV2 and Q25BV3 and Q25BV4, Q25BV9 and Q25BW0 and Q25BW2 and Q25BW3
;
NADH
Methylocystis sp.
-
-
NADH
Soil bacterium
-
-
NADPH
Q25BV2 and Q25BV3 and Q25BV4, Q25BV9 and Q25BW0 and Q25BW2 and Q25BW3
;
NADPH
Methylocystis sp.
-
-
NADPH
Soil bacterium
-
-
succinate
-
electron donor, membrane-bound enzyme
additional information
-
succinate, particulate enzyme functions in vitro with either succinate or NADH as electron donor, soluble enzyme functions only with NADH
-
additional information
-
-
-
additional information
-
duroquinol as artificial reductant
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Co2+
-
the enzyme contains three Co2+ ions per enzyme molecule
copper
-
the purified methane-oxidizing complex contains two copper atoms and one non-heme iron atom per mol of enzyme. The copper ion interacts with three or four nitrogenic ligands, EPR-active copper
copper
-
regulates the metabolic switch between the methane monooxygenase and the methane monooxygenase-NADH:quinone oxidoreductase complex, also regulates the level of expression of the pMMO and the development of internal membranes
copper
-
contains both mononuclear copper and a copper-containing cluster. Each 200000 Da pMMO complex contains 4.8 copper ions. The purified particulate methane monooxygenase is a mixture of Cu(I) and Cu(II) oxidation states
copper
-
required, activates
copper
-
an anomalous site modeled as a dinuclear copper cluster. The mononuclear copper site is absent (one His is not conserved), and the zinc replaced by a copper ion
Cu+
-
pMMO, requirement for, contains 12-15 Cu+ ions per molecule of enzyme
Cu+
-
the C-terminal domain of PmoB in pMMO is a reservoir for Cu(I) with properties similar to those of the E-cluster copper ions in the intact holoenzyme
Cu2+
-
copper genetically regulates the enzyme activity of the soluble and membrane-bound form
Cu2+
Methylococcus capsulatus, Methylocystis sp.
-
the active enzyme contains approximately 15 copper atoms per mol
Cu2+
-
the active enzyme contains approximately 15 copper atoms per mol enzyme
Cu2+
-
14.5 atoms per molecule of enzyme pMMO, type II copper centre
Cu2+
-
pMMO contains tightly bound copper, EDTA has no effect
Cu2+
-
increases enzyme expression and activity of the enzyme in recombinant Rhodococcus erythropolis strain LSSE8-1
Cu2+
-
the enzyme contains a mononuclear copper center and a dinuclear copper center, Cu-Cu interaction occurs in all redox forms of the enzyme, usage of mixed-valent dinuclear Cu model compounds, [tris{(N'-tert-butylureaylato)-N-ethyl}aminatocopper(II)]2BF4, and [N-tert-butylurealylato-{2-(dimethylamino)ethyl}aminatocopper(II)]2BF4, which are blue, and purple samples of [Cu2(m-xylylenediaminebis(Kemps triacid imide))(my-OTf)(THF)2], and [Cu2(m-xylylenediaminebis(Kemps triacid imide))(my-O2CCF3)(THF)2], EXAFS and Fourier transformation analysis, detailed interaction analysis, overview
Cu2+
-
stimulation by methanobactin-Cu2+ complex, no activation in absence of methanobactin
Cu2+
-
contains a mononuclear and a dinculear Cu2+ center in the soluble domain of the 47 kDa subunit
Cu2+
-
multicopper enzyme, contains 3 Cu2+ ions per trimer, contains 13.6 copper atoms per protein complex
Cu2+
-
Cu2+ is involved in the active site of pMMOH
Cu2+
-
pMH contains 2-4 atoms of copper per a minimum molecular weight of 99 kDa
Cu2+
-
purified pMMO contains 2-3 coppers
Cu2+
E1CBW9, E1CBX0, E1CBX1
the enzyme possesses a dicopper center; the enzyme possesses a dicopper center; the enzyme possesses a dicopper center
Cu2+
-
the enzyme is stimulated by exogenous copper (348% activity at 0.4 mM)
Cu2+
-
multi-copper enzyme with 14.1 copper atoms per protein, highest specific activity is observed wit 0.04 mM Cu2+ in the growth medium
Cu2+
-
pMMO contains a dicopper center and a mononuclear copper center, As-isolated enzyme conatins 10.2 Cu2+ equivalents per 100 kDa pMMO
Cu2+
-
pmMO contains copper ions (150 nmol per mg protein in membrane fractions) that are required for its enzymatic activity. Some increase in pMMO activity is observed by adding CuSO4
Fe
-
pMMOH bears a binuclear iron valence site [Fe(III)-Fe(IV)]
Fe2+
Methylococcus capsulatus, Methylocystis sp.
-
the active enzyme contains 2 iron atoms per mol
Fe2+
-
the active enzyme contains 2 iron atoms per mol enzyme
Fe2+
-
the enzyme contains one Fe2+ ion per enzyme molecule
Fe2+
-
As-isolated enzyme conatins 1.31 Fe2+ equivalents per 100 kDa pMMO
Fe2+
-
pmMO contains 450 nmol Fe2+ per mg protein in membrane fractions
Fe3+
-
presence of an octahedral environment that may well be exchange-coupled to another paramagnetic species
Fe3+
-
contains a diiron(III) center
Iron
-
2.5 atoms per enzyme molecule of pMMO
Iron
-
the purified methane-oxidizing complex contains two copper atoms and one non-heme iron atom per mol of enzyme, contains EPR-silent iron
Iron
-
each 200000 Da pMMO complex contains 1.5 iron ions
Iron
-
pMH contains 1 or 2 atoms of nonheme iron
Mn2+
-
pMMO, low content
Zn2+
-
increases enzyme expression and activity of the enzyme in recombinant Rhodococcus erythropolis strain LSSE8-1
Zn2+
-
the enzyme contains a nonphysiological mononuclear zinc center
Zn2+
-
contains one Zn2+ ion in the transmembrane domain
Zn2+
-
pmMO contains 1.5 nmol Zn2+ per mg protein in membrane fractions
Mo2+
-
pMMO, low content
additional information
-
copper-induced iron-uptake
additional information
-
analysis of the oxidation states and coordination environments of the pMMO metal centers, overview
additional information
-
Zn2+ is not associated with purified pMMO
additional information
-
purified pMMO does not contain zinc in the trans-membrane domain
additional information
-
purified pMMO contains no iron per pMMO protomer
additional information
-
increase of activity is not observed by adding FeSO4
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-Heptyl-4-hydroxyquinoline-N-oxide
-
pMMO, at 0.05 mM
Acetylene
-
complete inhibition at 0.1 mM
Acetylene
-
is a competitive inhibitor of pMH, interacts with its substrate-binding center
Acetylene
-
4.3% residual activity at 10% (v/v)
copper
Q49104
copper contents per 100 kDa alphabetagamma protomer of 15-20, eight to ten, two to three and two. Mixture of Cu(I) and Cu(II), copper cluster with a short Cu-Cu distance of 2.51 A that increases to 2.65 A upon chemical reduction with dithionite. The pMMO contains a mononuclear type 2Cu(II) centre and some type of copper cluster
copper
-
contains approximately two copper ions per 100 kDa protomer, type 2 Cu(II) present as two distinct species, mixture of Cu(I) and Cu(II). Short Cu-Cu interaction at 2.51 A. Di-copper centre plays an important functional role in pMMO, whereas the mononuclear copper centre is not critical
copper
-
two-coordinate (His2) mononuclear copper site and an anomalous site modeled as a dinuclear copper cluster. The cluster has one Cu ion bound by two His imidazoles and another by an imidazole and amino group of the pmoB N-terminal His
cyanide
-
less than 2% residual activity at 2 mM
duroquinol
-
increasing duroquinol concentration above 70 mM causes almost total inhibition of enzyme activity
EDTA
-
18.1% residual activity at 1.5 mM
Fe2+
-
slightly, membrane-bound enzyme form
-
Fe2+
Q49104
0.75 to two iron ions per protomer. Di-iron may be the pMMO active site
-
H2O2
-
reversible inhibition of pMMO with H2O2 upon treatment of pMMO with H2O2 followed by the addition of catalase. H2O2 re-oxidizes the type 2 copper in pMMO reduced with duroquinol
Myxothiazol
-
pMMO, suicide substrate
NaCl
-
decrease in activity might be due to reduced enzyme solubility with increasing NaCl concentrations
propylene oxide
-
product inhibition at higher concentration
Zinc
Q49104
site within the membrane that can be occupied by zinc or copper
Zinc
-
a zinc site, probably adventitious, as the crystallization medium requires the metal. Purified pMMO does not contain zinc in the trans-membrane domain
additional information
-
no detectable iron
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
catalase
-
increases pMMO activity, catalyzes decomposition of H2O2, on pMMO activity
-
Cu2+
-
pMMO, optimal at 0.3 mM
Fe3+
-
pMMO, optimal at 5.0 mM
-
lauryl maltoside
-
the stimulatory effect of lauryl maltoside is responsible for the initial increase in duroquinol-dependent activity of the pellet, but no activity with NADH is observed after this solubilization
methanobactin-Cu2+ complex
-
stimulation by methanobactin-Cu2+ complex, no activation in absence of copper, methanobactin is isolated from Methylosinus trichosporium strain OB3b
-
additional information
-
pMMO with the full complement of copper ions does not require methanobactin for activity
-
additional information
-
the active center of pMH is located in the beta-subunit
-
additional information
-
no pMMO acivity is observed in the detergent-solubilized fraction in the presence of dithionite, ascorbate, or methyl viologen. No pMMO activity with duroquinol or NADH is observed after solubilization with Triton X-100, Tween 20, zwittergent 3-12, Nonidet-P40, or synperonic
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.011
-
-
purified enzyme form pMMO
0.011
-
-
crude extract, using propylene as substrate, in 25 mM MOPS buffer (pH 7.0), at 30C
0.012
-
-
purified enzyme, using propylene as substrate, in 25 mM MOPS buffer (pH 7.0), at 30C
0.034
-
-
purified enzyme, substrates propylene and duroquinol
0.0605
-
-
whole cells, substrate formate
0.114
-
-
membrane-bound enzyme, substrates propylene and duroquinol
0.16
-
-
purified enzyme
0.23
-
-
membrane-bound enzyme, substrates propylene and NADH
additional information
-
-
optimization of a coupled assay method with propylene as substrate and a duroquinol-based NADH regeneration system
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.2
7.3
-
assay at
7.2
-
-
assay at
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
additional information
Soil bacterium
-
from microorganisms from arid and hyperarid soils in the Negev Desert, Israel
Manually annotated by BRENDA team
additional information
D0FK34, D0FK37, D0FK39, D0FK43, D0FK44, D0FK45, D0FK53, D0FK57, D0FK58, D0FK59, D0FK61, D0FK62, D0FK63, D0FK65, D0FK67, D0FKJ4, D0FKK3, D0FKS0, D0FL26, D0FL48
from aerobic methanotrophic community of a smooth-functioning biogas plant running on cattle dung; from aerobic methanotrophic community of a smooth-functioning biogas plant running on cattle dung; from aerobic methanotrophic community of a smooth-functioning biogas plant running on cattle dung; from aerobic methanotrophic community of a smooth-functioning biogas plant running on cattle dung; from aerobic methanotrophic community of a smooth-functioning biogas plant running on cattle dung; from aerobic methanotrophic community of a smooth-functioning biogas plant running on cattle dung; from aerobic methanotrophic community of a smooth-functioning biogas plant running on cattle dung; from aerobic methanotrophic community of a smooth-functioning biogas plant running on cattle dung; from aerobic methanotrophic community of a smooth-functioning biogas plant running on cattle dung; from aerobic methanotrophic community of a smooth-functioning biogas plant running on cattle dung; from aerobic methanotrophic community of a smooth-functioning biogas plant running on cattle dung; from aerobic methanotrophic community of a smooth-functioning biogas plant running on cattle dung; from aerobic methanotrophic community of a smooth-functioning biogas plant running on cattle dung; from aerobic methanotrophic community of a smooth-functioning biogas plant running on cattle dung; from aerobic methanotrophic community of a smooth-functioning biogas plant running on cattle dung; from aerobic methanotrophic community of a smooth-functioning biogas plant running on cattle dung; from aerobic methanotrophic community of a smooth-functioning biogas plant running on cattle dung; from aerobic methanotrophic community of a smooth-functioning biogas plant running on cattle dung; from aerobic methanotrophic community of a smooth-functioning biogas plant running on cattle dung; from aerobic methanotrophic community of a smooth-functioning biogas plant running on cattle dung
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
enzyme from cells grown under conditions of low copper availability
Manually annotated by BRENDA team
-
cytoplasmatic, soluble enzyme form termed sMMO
Manually annotated by BRENDA team
Methylococcus capsulatus Bath
-
cytoplasmatic, soluble enzyme form termed sMMO; sMMO
-
Manually annotated by BRENDA team
-
enzyme from cells grown under conditions of high copper availability is membrane-bound
Manually annotated by BRENDA team
-
membrane-bound particulate enzyme form termed pMMO
Manually annotated by BRENDA team
-
membrane-bound particulate enzyme form termed pMMO
Manually annotated by BRENDA team
-
enzyme from cells grown under conditions of high copper availability is membrane-bound; membrane-bound particulate enzyme form termed pMMO
Manually annotated by BRENDA team
-
intracytoplasmic membrane
Manually annotated by BRENDA team
-
integral membrane protein
Manually annotated by BRENDA team
Q25BV2 and Q25BV3 and Q25BV4, Q25BV9 and Q25BW0 and Q25BW2 and Q25BW3
;
Manually annotated by BRENDA team
Methylocystis sp.
-
-
Manually annotated by BRENDA team
E1CBW9, E1CBX0, E1CBX1
-
Manually annotated by BRENDA team
Methylococcus capsulatus ATCC 33009
-
-
-
Manually annotated by BRENDA team
Methylococcus capsulatus Bath
-
associated; associated; associated; bound, pMMO; bound to; enzyme from cells grown under conditions of high copper availability is membrane-bound; membrane-bound particulate enzyme form termed pMMO; membrane-bound particulate enzyme form termed pMMO
-
Manually annotated by BRENDA team
Methylococcus capsulatus HD6T
-
-
-
Manually annotated by BRENDA team
Methylococcus capsulatus M
-
bound
-
Manually annotated by BRENDA team
Methylomicrobium japanense NI
-
;
-
Manually annotated by BRENDA team
Methylosinus trichosporium IMV 3011
-
membrane-bound particulate enzyme form termed pMMO
-
Manually annotated by BRENDA team
additional information
-
two distinct enzyme forms exist: a soluble cytoplasmic sMMO and a membrane-bound particulate pMMO
-
Manually annotated by BRENDA team
additional information
Methylococcus capsulatus Bath
-
two distinct enzyme forms exist: a soluble cytoplasmic sMMO and a membrane-bound particulate pMMO
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
99000
-
-
pMMO, mass spectrometry
99000
-
-
SDS-PAGE
100000
-
-
apo-protein
200000
-
-
non-denaturing PAGE
220000
-
-
purified pMMO-detergent complex, gel filtration
390000
-
-
gel filtration
660000
-
-
solubilized enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
heterotrimer
-
1 * 45000 + 1 * 27000 + 1 * 23000, SDS-PAGE
heterotrimer
-
1 * 47000 + 1 * 24000 + 1 * 22000, X-ray crystallography
heterotrimer
-
1 * 42785 + 1 * 29733 + 1 * 28328, MALDI-TOF mass spectrometry
heterotrimer
-
1 * 47000 + 1 * 27000 + 1 * 25000, SDS-PAGE, pMMOH
heterotrimer
-
pMH, 1 * 47000, + 1 * 27000 + 1 * 25000, alphabetagamma-subunit, SDS-PAGE
heterotrimer
-
crystallography
heterotrimer
-
SDS-PAGE
heterotrimer
-
1 * 42785 + 1 * 29073 + 1 * 28328, MALDI-TOF mass spectrometry; 1 * 42786 + 1 * 29063 + 1 * 28376, calculated from amino acid sequence; 1 * 45000 + 1 * 27000 + 1 * 23000, SDS-PAGE
heterotrimer
-
1 * 40000 + 1 * 24000 + 1 * 21000, SDS-PAGE
heterotrimer
Methylococcus capsulatus ATCC 33009
-
1 * 42785 + 1 * 29073 + 1 * 28328, MALDI-TOF mass spectrometry; 1 * 42786 + 1 * 29063 + 1 * 28376, calculated from amino acid sequence; 1 * 45000 + 1 * 27000 + 1 * 23000, SDS-PAGE
-
heterotrimer
Methylococcus capsulatus Bath
-
1 * 45000 + 1 * 27000 + 1 * 23000, SDS-PAGE
-
heterotrimer
Methylococcus capsulatus M
-
1 * 47000 + 1 * 27000 + 1 * 25000, SDS-PAGE, pMMOH; pMH, 1 * 47000, + 1 * 27000 + 1 * 25000, alphabetagamma-subunit, SDS-PAGE
-
heterotrimer
-
1 * 45000 + 1 * 27000 + 1 * 23000, SDS-PAGE
-
hexamer
-
alpha2beta2gamma2
oligomer
-
x * 47000 + x * 26000 + x * 23000, SDS-PAGE
oligomer
Methylococcus capsulatus M
-
x * 47000 + x * 26000 + x * 23000, SDS-PAGE
-
trimer
-
1 * 47000 + 1 * 27000 + 1 * 25000, pMMO, mass spectrometry and SDS-PAGE
trimer
-
1 * 45000 + 1 * 26000 + 1 * 23000, pMMO, SDS-PAGE
trimer
-
1 * 47000 + 1 * 26000 + 1 * 23000, three-dimensional structure analysis of purified pMMO by electron microscopy and single-particle analysis at 23 A resolution, overview
trimer
Methylococcus capsulatus Bath
-
1 * 45000 + 1 * 26000 + 1 * 23000, pMMO, SDS-PAGE; 1 * 47000 + 1 * 26000 + 1 * 23000, three-dimensional structure analysis of purified pMMO by electron microscopy and single-particle analysis at 23 A resolution, overview; 1 * 47000 + 1 * 27000 + 1 * 25000, pMMO, mass spectrometry and SDS-PAGE
-
hexamer
Methylococcus capsulatus Bath
-
alpha2beta2gamma2
-
additional information
-
pMMO subunit A has acetylene binding ability
additional information
Methylococcus capsulatus Bath
-
pMMO subunit A has acetylene binding ability
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
heterotrimer of three subunits, pmoA, pmoB, and pmoC, with a solvent-exposed domain above the trans-membrane domain, which consists of alpha-helices
-
to 2.8 A resolution
Q49104
hanging drop vapor diffusion method
-
to 3.9 A resolution
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.8
-
-
or below: pMMO is irreversibly inactivated
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
pMMO is very unstable in vitro
-
copper ions increase the stability of exfoliated pMMO
-
instability of enzyme in crude extract
-
succinate stabilizes the membrane-bound enzyme
-
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
sensitive to O2, 3 kinetically distinct froms of pMMO with respect to O2 tension, type I is stable with moderate activity, type II is highly unstable to oxygen, type III is an intermediate form
-
438952
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-80C, pMMO is stable to proteolysis for many months
-
-80C, pMMO kinetically type I with respect to O2-sensitivity, repeated freeze-thaw-cycles, stable
-
4C, pMMO is stable to proteolysis for 1-2 weeks
-
4C, reducing argon or nitrogen atmosphere, no loss of activity after 1 week
-
4C, membrane-bound enzyme, activity is lost after 24 h, can be stabilized by succinate
-
4C, pMMO in membrane fractions under nitrogen atmosphere, 4 days, 20% loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
DEAE-Sepharose Fast Flow column chromatography, lysine agarose column chromatography, Sephacryl S-300HR gel filtration, QEA-Sephadex A-50 column chromatography, and Sephacryl S200 gel filtration, Superdex 200 gel filtration, or ammonium sulfate precipitation followed by Source 30Q column chroamtography
-
FPLC liquid chromatography and Mono Q HR 5/50 GL column chromatography
-
membrane-associated methane-oxidizing complex consisting of the particulate methane mono-oxygenase, pMMOH, and an unidentified component, assigned as a potential particulate methane mono-oxygenase reductase, pMMOR
-
Ni2+-Sepharose Fast Flow column chromatography
-
optimization of solubilization and purification procedure for the hydroxylase component of membrane-bound enzyme, purification to homogeneity involves solubilization by dodexylbeta-D-maltoside, ion exchange chromatography and gel filtration, the purification includes the loss of the reductase component
-
partially by preparation of washed membranes
-
particulate form of methane hydroxylase (pMH) obtained by ion exchange and hydrophobic chromatography
-
pMMO after induction with copper, kinetic type I with respect to O2-sensitivity
-
stable and active native pMMO from membranes, by solubilization with 1% w/v CHAPS, removal of soluble proteins, gel filtration, anion exchange chromatography, and ultrafiltration
-
POROS 20HQ column chromatography, gel filtration. Purified pMMO is inherently instable in vitro
-
by centrifugation and gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) or Rosetta (DE3) pLysS cells
-
genetic analysis of pMMO genes
-
two aqueous-exposed subdomains toward the N- and C-termini of the large subunit are expressed in Escherichia coli BL21 (DE3) cells
-
expressed in Escherichia coli
Methylocystis sp., Methylomicrobium album
-
DNA and amino acid sequence determination and anaylsis, the gene is organized in the structural gene cluster pmoCAB, stable functional expression of the membrane-bound enzyme in Rhodococcus erythropolis strain LSSE8-1 by using the dsz promoter and ethane as the sole carbon source, method optimization, overview
-
-
E1CBW9, E1CBX0, E1CBX1
pmoA cloned in pGEM-T Easy vector and transformed into Escherichia coli JM109 high-efficiency competent cells; pmoA cloned in pGEM-T Easy vector and transformed into Escherichia coli JM109 high-efficiency competent cells; pmoA cloned in pGEM-T Easy vector and transformed into Escherichia coli JM109 high-efficiency competent cells; pmoA cloned in pGEM-T Easy vector and transformed into Escherichia coli JM109 high-efficiency competent cells; pmoA cloned in pGEM-T Easy vector and transformed into Escherichia coli JM109 high-efficiency competent cells; pmoA cloned in pGEM-T Easy vector and transformed into Escherichia coli JM109 high-efficiency competent cells; pmoA cloned in pGEM-T Easy vector and transformed into Escherichia coli JM109 high-efficiency competent cells; pmoA cloned in pGEM-T Easy vector and transformed into Escherichia coli JM109 high-efficiency competent cells; pmoA cloned in pGEM-T Easy vector and transformed into Escherichia coli JM109 high-efficiency competent cells; pmoA cloned in pGEM-T Easy vector and transformed into Escherichia coli JM109 high-efficiency competent cells; pmoA cloned in pGEM-T Easy vector and transformed into Escherichia coli JM109 high-efficiency competent cells; pmoA cloned in pGEM-T Easy vector and transformed into Escherichia coli JM109 high-efficiency competent cells; pmoA cloned in pGEM-T Easy vector and transformed into Escherichia coli JM109 high-efficiency competent cells; pmoA cloned in pGEM-T Easy vector and transformed into Escherichia coli JM109 high-efficiency competent cells; pmoA cloned in pGEM-T Easy vector and transformed into Escherichia coli JM109 high-efficiency competent cells; pmoA cloned in pGEM-T Easy vector and transformed into Escherichia coli JM109 high-efficiency competent cells; pmoA cloned in pGEM-T Easy vector and transformed into Escherichia coli JM109 high-efficiency competent cells; pmoA cloned in pGEM-T Easy vector and transformed into Escherichia coli JM109 high-efficiency competent cells; pmoA cloned in pGEM-T Easy vector and transformed into Escherichia coli JM109 high-efficiency competent cells; pmoA cloned in pGEM-T Easy vector and transformed into Escherichia coli JM109 high-efficiency competent cells
D0FK34, D0FK37, D0FK39, D0FK43, D0FK44, D0FK45, D0FK53, D0FK57, D0FK58, D0FK59, D0FK61, D0FK62, D0FK63, D0FK65, D0FK67, D0FKJ4, D0FKK3, D0FKS0, D0FL26, D0FL48
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
the pMMO enzyme is expressed in cells grown under high copper-to-biomass ratios
-
pMMO is expressed at high copper/biomass ratios
-
pMMO is produced when the copper/biomass ratio is high
-
the pMMO enzyme is expressed in cells grown under high copper-to-biomass ratios
Methylococcus capsulatus Bath
-
-
pMMO is expressed at high copper/biomass ratios
Methylococcus capsulatus HD6T
-
-
the pMMO enzyme is expressed in cells grown under high copper-to-biomass ratios
Methylocystis sp.
-
the pMMO enzyme is expressed in cells grown under high copper-to-biomass ratios
-
-
the pMMO enzyme is expressed in cells grown under high copper-to-biomass ratios
-
the pMMO enzyme is expressed in cells grown under high copper-to-biomass ratios
-
-
pMMO is expressed at high copper/biomass ratios
-
for pMMO-expressing conditions, 0.02 mM copper is added and is equilibrated for at least 1 day before the media are inoculated
-
pMMO is expressed at high copper/biomass ratios
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
native occurence of a truncated form of pMMO with different molecular weight
additional information
Methylococcus capsulatus Bath
-
native occurence of a truncated form of pMMO with different molecular weight
-
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
copper ions increase the stability of exfoliated pMMO
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
degradation
-
pMMO can be used for biodegradation of mixtures of chlorinated solvents, i.e., trichloroethylene, trans-dichloroethylene, and vinyl chloride. If the concentrations are increased to 0.1 mM, pMMO-expressing cells grow faster and degrade more of these pollutants in a shorter amount of time than sMMO